Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Grazyna Leszczynska"'
Autor:
Patrycja Szczupak, Malgorzata Sierant, Ewelina Wielgus, Ewa Radzikowska-Cieciura, Katarzyna Kulik, Agnieszka Krakowiak, Paulina Kuwerska, Grazyna Leszczynska, Barbara Nawrot
Publikováno v:
Cells, Vol 11, Iss 9, p 1522 (2022)
The bacterial enzyme tRNA 2-selenouridine synthase (SelU) is responsible for the conversion of 5-substituted 2-thiouridine (R5S2U), present in the anticodon of some bacterial tRNAs, into 5-substituted 2-selenouridine (R5Se2U). We have already demonst
Externí odkaz:
https://doaj.org/article/3aeb9907943547ef934c4e0aa8fd7698
Publikováno v:
Molecules, Vol 27, Iss 1, p 133 (2021)
One-electron oxidation of 2-selenouracil (2-SeU) by hydroxyl (●OH) and azide (●N3) radicals leads to various primary reactive intermediates. Their optical absorption spectra and kinetic characteristics were studied by pulse radiolysis with UV-vis
Externí odkaz:
https://doaj.org/article/35f528458a1a4111a9fbb32615698590
Publikováno v:
Molecules, Vol 25, Iss 15, p 3344 (2020)
The chemical synthesis of modified oligoribonucleotides represents a powerful approach to study the structure, stability, and biological activity of RNAs. Selected RNA modifications have been proven to enhance the drug-like properties of RNA oligomer
Externí odkaz:
https://doaj.org/article/d2fe50c855594a2682eb2dffc40863e6
Autor:
Grazyna Leszczynska, Marek Cypryk, Bartlomiej Gostynski, Klaudia Sadowska, Paulina Herman, Grzegorz Bujacz, Elzbieta Lodyga-Chruscinska, Elzbieta Sochacka, Barbara Nawrot
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 8, p 2882 (2020)
5-Substituted 2-selenouridines (R5Se2U) are post-transcriptional modifications present in the first anticodon position of transfer RNA. Their functional role in the regulation of gene expression is elusive. Here, we present efficient syntheses of 5-m
Externí odkaz:
https://doaj.org/article/673efc01bb074007a389d94ac951dc0f
Publikováno v:
Biomolecules, Vol 8, Iss 4, p 145 (2018)
Oxidative RNA damage is linked to cell dysfunction and diseases. The present work focuses on the in vitro oxidation of 5-methylaminomethyl uridine (mnm5U), which belongs to the numerous post-transcriptional modifications that are found in tRNA. The r
Externí odkaz:
https://doaj.org/article/942c431d4b774998a46812e3a470de7e
Publikováno v:
Organic & Biomolecular Chemistry. 21:2809-2815
5-CF3-pyrimidine ribonucleosides offer rapid, efficient and scalable C5 heteronucleobase functionality with carboxyl, nitrile, ester, amide and amidine groups.
Autor:
Katarzyna Kulik, Joanna Wasko, Barbara Nawrot, Karolina Podskoczyj, Tsutomu Suzuki, Grazyna Leszczynska
Publikováno v:
Chemical Communications. 57:12540-12543
A single point mutation (A4435G) in the human mitochondrial tRNAMet (hmt-tRNAMet) gene causes severe mitochondrial disorders associated with hypertension, type 2 diabetes and LHON. This mutation leads to the exchange of A37 in the anticodon loop of h
Autor:
Karolina, Podskoczyj, Katarzyna, Kulik, Joanna, Wasko, Barbara, Nawrot, Tsutomu, Suzuki, Grazyna, Leszczynska
Publikováno v:
Chemical communications (Cambridge, England). 57(93)
A single point mutation (A4435G) in the human mitochondrial tRNA
Publikováno v:
RSC Advances. 9:40507-40512
Two novel methods for the preparation of the virtually equimolar mixtures of (S)- and (R)-diastereomers of 5-methoxycarbonylhydroxymethyluridine (mchm5U) have been developed. The first method involved α-hydroxylation of a 5-malonate ester derivative
Autor:
Karolina Podskoczyj, Christophe Velours, Grazyna Leszczynska, Jingjing Zhou, Marine Lénon, Marc Fontecave, Jean-Luc Ravanat, Béatrice Golinelli-Pimpaneau, Nadia Touati, Frédéric Barras
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, 49 (7), pp.3997-4007. ⟨10.1093/nar/gkab138⟩
Nucleic Acids Research, 2021, 49 (7), pp.3997-4007. ⟨10.1093/nar/gkab138⟩
Nucleic Acids Research, Oxford University Press, 2021, 49 (7), pp.3997-4007. ⟨10.1093/nar/gkab138⟩
Nucleic Acids Research, 2021, 49 (7), pp.3997-4007. ⟨10.1093/nar/gkab138⟩
Sulfuration of uridine 34 in the anticodon of tRNAs is conserved in the three domains of life, guaranteeing fidelity of protein translation. In eubacteria, it is catalyzed by MnmA-type enzymes, which were previously concluded not to depend on an iron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bdf0079ecb321aef63f1441ad9814d5
https://hal.archives-ouvertes.fr/hal-03390337
https://hal.archives-ouvertes.fr/hal-03390337